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Title: Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition
Authors: Ravindran, Anita
Sze, Siu Kwan
Adav, Sunil S.
Keywords: DRNTU::Science::Biological sciences::Microbiology
Issue Date: 2013
Source: Adav, S. S., Ravindran, A., & Sze, S. K. (2013). Proteomic Analysis of Temperature Dependent Extracellular Proteins from Aspergillus fumigatus Grown under Solid-State Culture Condition. Journal of Proteome Research, 12(6), 2715-2731.
Series/Report no.: Journal of proteome research
Abstract: Fungal species of the genus Aspergillus are filamentous ubiquitous saprophytes that play a major role in lignocellulosic biomass recycling and also are considered as cell factories for the production of organic acids, pharmaceuticals, and industrially important enzymes. Analysis of extracellular secreted biomass degrading enzymes using complex lignocellulosic biomass as a substrate by solid-state fermentation could be a more practical approach to evaluate application of the enzymes for lignocellulosic biorefinery. This study isolated a fungal strain from compost, identified as Aspergillus fumigatus, and further analyzed it for lignocellulolytic enzymes at different temperatures using label free quantitative proteomics. The profile of secretome composition discovered cellulases, hemicellulases, lignin degrading proteins, peptidases and proteases, and transport and hypothetical proteins; while protein abundances and further their hierarchical clustering analysis revealed temperature dependent expression of these enzymes during solid-state fermentation of sawdust. The enzyme activities and protein abundances as determined by exponentially modified protein abundance index (emPAI) indicated the maximum activities at the range of 40–50 °C, demonstrating the thermophilic nature of the isolate A. fumigatus LF9. Characterization of the thermostability of secretome suggested the potential of the isolated fungal strain in the production of thermophilic biomass degrading enzymes for industrial application.
ISSN: 1535-3893
DOI: 10.1021/pr4000762
Fulltext Permission: none
Fulltext Availability: No Fulltext
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